Critical nucleation size in the folding of small apparently two-state proteins.

TitleCritical nucleation size in the folding of small apparently two-state proteins.
Publication TypeJournal Article
Year of Publication2004
AuthorsBai, Y, Zhou H, Zhou Y
JournalProtein science : a publication of the Protein Society
Volume13
Pagination1173-81
Date Published2004 May
Abstract

For apparently two-state proteins, we found that the size (number of folded residues) of a transition state is mostly encoded by the topology, defined by total contact distance (TCD) of the native state, and correlates with its folding rate. This is demonstrated by using a simple procedure to reduce the native structures of the 41 two-state proteins with native TCD as a constraint, and is further supported by analyzing the results of eight proteins from protein engineering studies. These results support the hypothesis that the major rate-limiting process in the folding of small apparently two-state proteins is the search for a critical number of residues with the topology close to that of the native state.

Pub Med Link

http://www.ncbi.nlm.nih.gov/pubmed/15075405?dopt=Abstract

Alternate JournalProtein Sci.
Citekey15075405